ArticleCell2018
Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.
Article in Cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
55 citing papers in PubMed, 115 citations in OpenAlex.
- Topogenic sequence recognition at TIM complexes revealed by a stendomycin-bound structure.Nature chemical biology · 2026Article
- Direct coupling of human TOM and TIM22 complexes drives mitochondrial carrier import.Nature structural & molecular biology · 2026Article
- Dynamic disorder is crucial for mitochondrial protein import.Protein science : a publication of the Protein Society · 2026Review
- From the cytosol to the inner membrane: biogenesis of the mitochondrial carrier family.Protein science : a publication of the Protein Society · 2026Review
- Functional Interaction Between Toc75 POTRA1 Domain and Tic22-III in the Intermembrane Space During Chloroplast Protein Import.Plant direct · 2026Article
- A dynamic displacement mechanism drives protein import into mitochondria.bioRxiv : the preprint server for biology · 2026Article
- Biogenesis and function of the mitochondrial solute carrier (SLC25) family in yeast.Biological chemistry · 2025Review
- Molecular machineries and pathways of mitochondrial protein transport.Nature reviews. Molecular cell biology · 2025Review
- Review
- Biogenesis of mitochondrial β-barrel membrane proteins.FEBS open bio · 2024Review
- Protein insertion into the inner membrane of mitochondria: routes and mechanisms.FEBS open bio · 2024Review
- Dual client binding sites in the ATP-independent chaperone SurA.Nature communications · 2024Article
- Is There a Mitochondrial Protection via Remote Ischemic Conditioning in Settings of Anticancer Therapy Cardiotoxicity?Current heart failure reports · 2024Review
- Structural basis of substrate recognition and allosteric activation of the proapoptotic mitochondrial HtrA2 protease.Nature communications · 2024Article
- Modular Assembly of Mitochondrial β-Barrel Proteins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Adenine nucleotide carrier protein dysfunction in human disease.IUBMB life · 2023Review
- Human Tim8a, Tim8b and Tim13 are auxiliary assembly factors of mature Complex IV.EMBO reports · 2023Article
- Thumb-domain dynamics modulate the functional repertoire of DNA-Polymerase IV (DinB).Nucleic acids research · 2023Article
- The Mechanism of Antimicrobial Activity of Conjugated Bile Acids against Lactic Acid Bacilli.Microorganisms · 2023Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 5 institutions in 3 countries.
Funding
Abstract
The exchange of metabolites between the mitochondrial matrix and the cytosol depends on β-barrel channels in the outer membrane and α-helical carrier proteins in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones escort these proteins through the intermembrane space, but the structural and mechanistic details remain elusive. We have used an integrated structural biology approach to reveal the functional principle of TIM chaperones. Multiple clamp-like binding sites hold the mitochondrial membrane proteins in a translocation-competent elongated form, thus mimicking characteristics of co-translational membrane insertion. The bound preprotein undergoes conformational dynamics within the chaperone binding clefts, pointing to a multitude of dynamic local binding events. Mutations in these binding sites cause cell death or growth defects associated with impairment of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial "transfer-chaperone" system is able to guide α-helical and β-barrel membrane proteins in a "nascent chain-like" conformation through a ribosome-free compartment.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.